Biophysical Journal 33: 63-79 (1981)
© 1981 the Biophysical Society

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by LaGattuta, K J Articles by Kothari, B K Search for Related Content PubMed PubMed Citation Articles by LaGattuta, K J Articles by Kothari, B K

Diffusion coefficients of hemoglobin by intensity fluctuation spectroscopy: effects of varying pH and ionic strength.

ABSTRACT

Measurements of the mutual diffusion coefficients (D) of the liganded human hemoglobins (Hb) oxy-HbA and oxy-HbS were performed as a function of Hb concentration (CHb), pH, and ionic strength (tau) by intensity fluctuation spectroscopy (IFS). Average diffusion coefficients, (D), and normalized variances, ((D/(D) - 1)2), were recorded. Results are reported and select features are discussed quantitatively. (a) for tau = 0.15 M, the shape of the (d) vs. CHb curve is found to vary with pH. We developed a precise description of this effect in the form of an algebraic relationship between (D), CHb, and Z, the titration charge. (b) only slight differences between the (D) values of oxy-HbS and oxy-HbA are observed, at tau = 0.15 M, for CHb Less Than or Equal To 10 g%. These differences are explained by the theory of part a. (c) No evidence of aggregation is found in solutions of oxy-HbA or oxy-HbS, at tau = 0.15 M, for CHb Less Than or Equal To 10 g%. (d) Indications of aggregation appear in oxy-HbA solutions at very low concentrations of salt. An estimate is made of the extent of aggregation, and the average radius of a cluster is determined.